Synthetic and biological approaches to map substrate specificities of proteases
| Autor: | Joshua J. Yim, Shiyu Chen, Matthew Bogyo |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Proteases medicine.medical_treatment Clinical Biochemistry Peptide Computational biology Biology Proteomics 01 natural sciences Biochemistry Substrate Specificity Biological pathway 03 medical and health sciences medicine Humans Protease Inhibitors Molecular Biology chemistry.chemical_classification Protease 010405 organic chemistry Antigen processing Active site 0104 chemical sciences 030104 developmental biology chemistry biology.protein Peptides Function (biology) Peptide Hydrolases Signal Transduction |
| Zdroj: | Biological Chemistry. 401:165-182 |
| ISSN: | 1437-4315 1431-6730 |
| DOI: | 10.1515/hsz-2019-0332 |
| Popis: | Proteases are regulators of diverse biological pathways including protein catabolism, antigen processing and inflammation, as well as various disease conditions, such as malignant metastasis, viral infection and parasite invasion. The identification of substrates of a given protease is essential to understand its function and this information can also aid in the design of specific inhibitors and active site probes. However, the diversity of putative protein and peptide substrates makes connecting a protease to its downstream substrates technically difficult and time-consuming. To address this challenge in protease research, a range of methods have been developed to identify natural protein substrates as well as map the overall substrate specificity patterns of proteases. In this review, we highlight recent examples of both synthetic and biological methods that are being used to define the substrate specificity of protease so that new protease-specific tools and therapeutic agents can be developed. |
| Databáze: | OpenAIRE |
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